Proteolytic enzyme activity in rat hindlimb muscles in fetus and during post-natal development.
The enzymatic activity of two lysosomal enzymes, acid phosphatase and cathepsin D, was determined in fetus and during post-natal development of the rat gastrocnemius muscle in comparison to the histological differentiation of this muscle. The specific activity of cathepsin D and acid phosphatase was 7 and 2.5 fold higher in the muscle during development until 20 days after birth, than that of mature muscle, respectively. A trend of gradual decrease in the activity of these enzymes was observed concomitantly with the differentiation and maturation of the muscle from mononucleated cells in the fetus to myotubes formation at day 1 after birth, followed by the formation of "young" and then striated myofibers in 10- and 20-day old neonates, respectively. However, no correlation could be found between the lysosomal enzyme activity and the developmental stages of the muscle until 20 days after birth. It is suggested that the elevated activity of lysosomal acid hydrolases may be associated with late developmental processes from young to mature myofibers in normal skeletal muscle and not only in various pathological conditions.
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Department of Zoology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Israel.
D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D002402:Cathepsin D / Q000378:metabolism; D006614:Hindlimb; D008247:Lysosomes / Q000201:enzymology; D024510:Muscle Development; D009132:Muscles / Q000196:embryology / Q000201:enzymology*; D051381:Rats
D000135:Acid Phosphatase; D002402:Cathepsin D